Proteomics

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K63-Linked Ubiquitylation of S2P-RNAPII Regulates Transcription in a DNA-PK Inter-Dependent Manner in Response to Double-Strand Breaks

ABSTRACT: The goal of this experiment was to conduct immunoprecipitation (IP) on lysates from control and neocarzinostatin (NCS)-treated U2OS cells (at 30 minutes and 2 hours) to identify the proteins that interact with Polr2a and to investigate how NCS treatment influences the relative abundance of Polr2a and its interacting proteins.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Adam Pap  

LAB HEAD: Tibor Pankotai

PROVIDER: PXD059497 | Pride | 2026-05-25

REPOSITORIES: Pride

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Dataset's files

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Action DRS
L_E_F_240506_CTRL_IgG_07.mgf Mgf
L_E_F_240506_CTRL_IgG_07.msf Msf
L_E_F_240506_CTRL_IgG_07.raw Raw
L_E_F_240506_CTRL_S2P_10.mgf Mgf
L_E_F_240506_CTRL_S2P_10.msf Msf
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K63-linked ubiquitylation of S2P-RNAPII regulates transcription in a DNAPK inter-dependent manner in response to double-strand breaks.

Pantazi Vasiliki V   Smith Paul P   Pahi Zoltan G ZG   Katona Manuela M   Pap Adam A   Darula Zsuzsanna Z   Fischer Roman R   Vendrell Iolanda I   Kessler Benedikt M BM   van Vugt Marcel A T M MATM   D'Angiolella Vincenzo V   Pankotai Tibor T  

Nucleic acids research 20260401 8

DNA double-strand breaks (DSBs) are highly toxic DNA lesions that can lead to genomic instability. DSBs can also interfere with other DNA-based processes, including transcription, and thereby jeopardizing cellular function. In situations of persistent DSBs, RNA polymerase II (RNAPII) needs to be removed to facilitate DNA repair. DSB-induced RNAPII removal involves multifaceted ubiquitylation, but the mechanisms involved remain elusive. Our data show that in response to DSBs, the E3 ubiquitin lig  ...[more]

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